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Two successive and selective coacervations induced by chitosan (Ch) and carrageenan (CG) were applied to remove antinutritional protease inhibitors and purify Bowman–Birk protease inhibitor (BBI) from soybean whey. At the first coacervation induced by Ch (66.7, 200, and 510kDa), only Kunitz trypsin inhibitor (KTI) and BBI complexed with Ch were extracted, while β-amylase and soybean agglutinin remained...
Proteins in soybean whey were separated into two groups by graded salt precipitation, low and high isoelectric point protein fractions (LIP and HIP), corresponding to the mixture of Kunitz trypsin inhibitor (KTI) and Bowman–Birk protease inhibitor (BBI) as well as the mixture of soybean agglutinin (SBA) and β-amylase, respectively. The complex behavior of LIP and HIP with ι-carrageenan (CG) as a function...
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